The breast cancer susceptibility gene contains at its C-terminus two copies of
a conserved domain that was named BRCT for BRCA1 C-terminus. This domain of
about 95 amino acids exists in a large number of proteins from prokaryotes to
eukaryotes. BRCT domain-containing proteins are involved in multiple cellular
responses, including cell cycle checkpoint control, DNA repair, and
transcription regulation [1,2,3]. The BRCT domain is not limited to the C-termini of protein sequences and can be found in multiple copies or in a
single copy as in RAP1 and TdT. Aside from a role as phospho-peptide modules,
BRCT domains have been implicated in phosphorylation-independent protein
interactions, DNA binding and poly(ADP-ribose) (PAR) binding [4,5].
The BRCT domain fold is comprised of a central 4-stranded β-sheet flanked
by a single α-helix (α2) on one side and two α-helices (α1
and α3) on the opposite side (see <PDB:1CDZ>) [5,6].
Some proteins known to contain a BRCT domain are listed below:
Mammalian breast cancer type 1 susceptibility protein. It may regulate gene
Human p53-binding protein 1.
Human poly(ADP-ribose) polymerase (PARP) (EC 188.8.131.52). It modifies various
nuclear proteins by poly(ADP-rybosyl)ation.
Vertebrate DNA nucleotidylexotransferase (EC 184.108.40.206). It adds nucleotides
at the junction (N region) of rearranged Ig heavy chain and T cell receptor
gene segments during the maturation of B and T cells.
Mammalian DNA-repair protein XRCC1.
Human DNA ligase III (EC 220.127.116.11). It is involved in DNA strand-break
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see prosite_license.html.